The dissociation properties of native C1.

Détails

ID Serval
serval:BIB_5A845EEEAEB4
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The dissociation properties of native C1.
Périodique
Biochemical and Biophysical Research Communications
Auteur(s)
Ziccardi R.J., Tschopp J.
ISSN
0006-291X (Print)
ISSN-L
0006-291X
Statut éditorial
Publié
Date de publication
1982
Volume
107
Numéro
2
Pages
618-623
Langue
anglais
Résumé
The first component of human complement (C1) readily dissociates under physiologic conditions into two subunits - C1q and C1r2C1s2. The equilibrium constant for this reaction has been determined for native C1 in fresh normal human serum by hemolytic titration. Standard technology was modified to simulate physiologic conditions. Furthermore, assays were carried out at numerous poncentrations of sensitized erythrocytes, thereby allowing the calculation of the percent of associated C1 at different total C1 concentration. Increased C1 dissociation was observed with dilution. From these data, an association constant of 4.5 × 108 M−1 was calculated for native C1. Thus in normal human serum approximately ten percent of the C1 is present as free C1q and C1r2C1s2.
Mots-clé
Complement Activating Enzymes/analysis, Complement C1/analysis, Complement C1q, Complement C1r, Complement C1s, Humans, Macromolecular Substances, Mathematics
Pubmed
Web of science
Création de la notice
24/01/2008 15:18
Dernière modification de la notice
20/08/2019 14:13
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